Sandbox 47
From Proteopedia
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BPTI is a single chain polypeptide with 58 amino acids. It's secondary structure includes one <scene name='Sandbox_47/Sheet_ribbon/1'>beta sheet</scene> and <scene name='Sandbox_47/Helices/1'>two alpha helices</scene>. The beta sheet consists of <scene name='Sandbox_47/Sheet_side_chains/1'>two antiparallel strands</scene> (Ile18 to Asn 24 and Leu 29 to Tyr 35) with a <scene name='Sandbox_47/Turn/1'>beta hairpin</scene> consisting of four residues (Ala 25, Lys 26, Ala 27, Gly 28). Alpha helix | BPTI is a single chain polypeptide with 58 amino acids. It's secondary structure includes one <scene name='Sandbox_47/Sheet_ribbon/1'>beta sheet</scene> and <scene name='Sandbox_47/Helices/1'>two alpha helices</scene>. The beta sheet consists of <scene name='Sandbox_47/Sheet_side_chains/1'>two antiparallel strands</scene> (Ile18 to Asn 24 and Leu 29 to Tyr 35) with a <scene name='Sandbox_47/Turn/1'>beta hairpin</scene> consisting of four residues (Ala 25, Lys 26, Ala 27, Gly 28). Alpha helix | ||
<scene name='Sandbox_47/H1/1'>H1</scene> is 4 residues (Asp 3 to Cys 6), and <scene name='Sandbox_47/H2/1'>H2</scene> is 8 residues (Ala 48 to Cys 55). There are three intrachain disulfide bonds in this polypeptide, one between <scene name='Sandbox_47/Ds1/1'>Cys 5 and Cys 55</scene>, one between <scene name='Sandbox_47/Ds2/1'>Cys 14 and Cys 38</scene>, and one between <scene name='Sandbox_47/Ds3/1'>Cys 30 and Cys 51</scene>. This protein has a <scene name='Sandbox_47/Hydrophobic_core/1'>hydrophobic core</scene> (gray) with polar and charged residues (purple) extending mostly on the <scene name='Sandbox_47/Hydrophobic_dist/3'>surface</scene>. | <scene name='Sandbox_47/H1/1'>H1</scene> is 4 residues (Asp 3 to Cys 6), and <scene name='Sandbox_47/H2/1'>H2</scene> is 8 residues (Ala 48 to Cys 55). There are three intrachain disulfide bonds in this polypeptide, one between <scene name='Sandbox_47/Ds1/1'>Cys 5 and Cys 55</scene>, one between <scene name='Sandbox_47/Ds2/1'>Cys 14 and Cys 38</scene>, and one between <scene name='Sandbox_47/Ds3/1'>Cys 30 and Cys 51</scene>. This protein has a <scene name='Sandbox_47/Hydrophobic_core/1'>hydrophobic core</scene> (gray) with polar and charged residues (purple) extending mostly on the <scene name='Sandbox_47/Hydrophobic_dist/3'>surface</scene>. | ||
| - | BPTI interacts with 98 <scene name='Sandbox_47/Water/1'>water molecules</scene> as well as 4 <scene name='Sandbox_47/Ligands/1'>sulfate anion ligands</scene>. | + | BPTI interacts with 98 <scene name='Sandbox_47/Water/1'>water molecules</scene> as well as 4 <scene name='Sandbox_47/Ligands/1'>sulfate anion ligands</scene>. Ligand <scene name='Sandbox_47/Ligand_61/1'>61 A</scene> binds the protein through hydrophobic interactions between Glu 7, Lys 7, and Phe 41, as well as through 3 hydrogen bonds to Arg 42. Three water molecules are also interact with this ligand. |
Revision as of 19:15, 29 October 2010
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
Bovine Pancreatic Trypsin Inhibitor (BPTI) Mutant with Altered Binding Loop Sequence
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BPTI is a single chain polypeptide with 58 amino acids. It's secondary structure includes one and . The beta sheet consists of (Ile18 to Asn 24 and Leu 29 to Tyr 35) with a consisting of four residues (Ala 25, Lys 26, Ala 27, Gly 28). Alpha helix is 4 residues (Asp 3 to Cys 6), and is 8 residues (Ala 48 to Cys 55). There are three intrachain disulfide bonds in this polypeptide, one between , one between , and one between . This protein has a (gray) with polar and charged residues (purple) extending mostly on the . BPTI interacts with 98 as well as 4 . Ligand binds the protein through hydrophobic interactions between Glu 7, Lys 7, and Phe 41, as well as through 3 hydrogen bonds to Arg 42. Three water molecules are also interact with this ligand.
